Interaction and binding mechanism of lipid oxidation products to sturgeon myofibrillar protein in low temperature vacuum heating conditions: Multispectroscopic and molecular docking approaches.
Food Chem X
; 15: 100389, 2022 Oct 30.
Article
in En
| MEDLINE
| ID: mdl-36211750
ABSTRACT
In this work, the binding mechanism of myofibrillar protein (MP) with malondialdehyde and 4-hydroxy-2-nonenal under low temperature vacuum heating was investigated via multispectroscopic and molecular docking. The results showed that binding interaction and increasing temperature caused significant changes in the conformations as well as a decrease in the value of protein intrinsic fluorescence, surface hydrophobicity, and fluorescence excitation-emission matrix spectra. Furthermore, the decrease in α-helix and ß-turn, increase in ß-sheet and a random coil of MP, imply the MP molecules to be more unfolded. Isothermal titration calorimetry and molecular docking results showed that main driving force for binding with MP was hydrogen bond, and the binding ability of malondialdehyde was superior to that of 4-hydroxy-2-nonenal. Moreover, increasing the heating temperature was beneficial to the binding reaction and intensified the conformational transition of MP. These results will provide a reference for further studies on the lipid and protein interaction of sturgeon.
4-Hydroxy-2-nonenal; Binding mechanism; HNE, 4-hydroxy Nonenal; ITC, isothermal titration calorimetry; LTVH, low temperature vacuum heating; Low temperature vacuum heating; MDA, malondialdehyde; MP, myofibrillar protein; Malondialdehyde; Molecular docking; Sturgeon myofibrillar protein; Trp, tryptophan; Tyr, tyrosine
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Language:
En
Journal:
Food Chem X
Year:
2022
Document type:
Article